The goal of our research is to enhance understanding of the behavior of chemical systems relevant to biochemistry. A wide variety of methods including 1H and 13C NMR, ESR, kinetics, polarimetry, and UV and IR spectroscopy are being used to study fast proton transfers, normal and inverted micelles, hydrocarbon-water boundaries, enzyme models, thermochromic and charge-transfer systems, and microemulsions. For example, we are investigating micellar aggregates with respect to water penetration, surface roughness, adsorption sites, interior viscosity, chain conformation, and ion binding. We have also solubilized an enzyme, gamma-chymotrypsin, inside inverted micelles ("water pools") and have found that this enzyme functions rather normally in solvent systems containing only 2% water and 98% heptane. In addition, we have just completed a study of conformation equilibria at micelle surfaces in which the rotamer stability of long-chain amino acid derivatives was determined in the micellar state. The stereochemistry of solvolyses of chiral substrates at interfaces in microemulsions is also being investigated.